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Host-selected amino acid changes at the sialic acid binding pocket of the parvovirus capsid modulate cell binding

Alberto López-Bueno1, Mari-Paz Rubio, Nathan Bryant

  • 1Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Universidad Autónoma de Madrid, 28049 Cantoblanco, Madrid, Spain.

Journal of Virology
|January 18, 2006
PubMed

Insights

Viral capsid mutations influence receptor binding and pathogenicity. Changes in minute virus of mice (MVMp) capsid proteins alter sialic acid interactions, leading to lethal disease in mice and revealing a key mechanism for parvovirus evolution.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Evolution

Background:

  • Parvoviruses, including minute virus of mice (MVMp), can adapt and increase virulence.
  • Receptor recognition is crucial for viral entry and host adaptation.

Purpose of the Study:

  • To investigate how receptor recognition influences the emergence of virulent parvoviruses.
  • To identify specific capsid mutations in MVMp responsible for increased pathogenicity.

Main Methods:

  • Genetic analysis of MVMp viral clones isolated from infected mice.
  • Construction and characterization of recombinant MVMp viruses with specific capsid mutations.
  • In vitro cell-based assays (cytotoxicity, neuraminidase treatment) and in vivo infection models (SCID mice).
  • X-ray crystallography of MVMp capsids bound to sialic acid.

Main Results:

  • Single amino acid substitutions (V325M, I362S, K368R) in MVMp capsid proteins were identified in virulent clones.
  • Mutant viruses exhibited altered cell binding avidity and increased sensitivity to neuraminidase, indicating reduced affinity for sialic acid receptors.
  • Recombinant viruses with these mutations caused lethal disease in SCID mice.
  • X-ray crystal structure revealed sialic acid binding near residues I362 and K368 in the capsid's dimple region.

Conclusions:

  • Specific MVMp capsid mutations directly impact sialic acid receptor interactions.
  • Altered receptor binding affinity is a key factor regulating parvovirus pathogenicity and host adaptation.
  • This study provides the first crystal structure of a parvovirus capsid with an identified infectious receptor attachment site.

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